ID K3W6I2_GLOUD Unreviewed; 1384 AA.
AC K3W6I2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Globisporangium ultimum (strain ATCC 200006 / CBS 805.95 / DAOM BR144)
OS (Pythium ultimum).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae;
OC Globisporangium.
OX NCBI_TaxID=431595 {ECO:0000313|EnsemblProtists:PYU1_T000573, ECO:0000313|Proteomes:UP000019132};
RN [1] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RX PubMed=20626842; DOI=10.1186/gb-2010-11-7-r73;
RA Levesque C.A., Brouwer H., Cano L., Hamilton J.P., Holt C., Huitema E.,
RA Raffaele S., Robideau G.P., Thines M., Win J., Zerillo M.M., Beakes G.W.,
RA Boore J.L., Busam D., Dumas B., Ferriera S., Fuerstenberg S.I.,
RA Gachon C.M., Gaulin E., Govers F., Grenville-Briggs L., Horner N.,
RA Hostetler J., Jiang R.H., Johnson J., Krajaejun T., Lin H., Meijer H.J.,
RA Moore B., Morris P., Phuntmart V., Puiu D., Shetty J., Stajich J.E.,
RA Tripathy S., Wawra S., van West P., Whitty B.R., Coutinho P.M.,
RA Henrissat B., Martin F., Thomas P.D., Tyler B.M., De Vries R.P., Kamoun S.,
RA Yandell M., Tisserat N., Buell C.R.;
RT "Genome sequence of the necrotrophic plant pathogen Pythium ultimum reveals
RT original pathogenicity mechanisms and effector repertoire.";
RL Genome Biol. 11:R73-R73(2010).
RN [2] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RA Buell R., Hamilton J., Hostetler J.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:PYU1_T000573}
RP IDENTIFICATION.
RC STRAIN=DAOM BR144 {ECO:0000313|EnsemblProtists:PYU1_T000573};
RG EnsemblProtists;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; GL376636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 431595.K3W6I2; -.
DR EnsemblFungi; PYU1_T000573; PYU1_T000573-p1; PYU1_G000573.
DR EnsemblProtists; PYU1_T000573; PYU1_T000573; PYU1_G000573.
DR VEuPathDB; FungiDB:PYU1_G000573; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; K3W6I2; -.
DR OMA; DMMIYQR; -.
DR Proteomes; UP000019132; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000019132};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 192..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 400..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 451..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 994..1012
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1024..1046
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1077..1099
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1114..1132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1139..1158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1178..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 127..189
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 963..1215
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1384 AA; 154047 MW; B91CB86F1729BE2C CRC64;
MASKGRLFGG GGPRVEDEEL LRHQTRSTSA GSNPPLLTKE SNSSSDYVYA EMGSPALLQQ
PQRIGDADDS GRHKRTLTGG GGGGKLPATK NRGNSRTGPA AVGHDYSNNN NGGGDSDKAK
QELREVYFNY APGNAVFDKS TNVVITSKYN VLTFLPKFLK ESFTKVANFF FLVVCVLQSI
DSISNTYGVP TNAPVLLFVI SIDAVFAIME DMRRHTSDRE ANSAKCHIVR NGHIEDHLWS
EVKVGDFLQI RNREVIPADV LILSVSEPVG EAASGICYVE TKSLDGETNL KLRQAIQPTM
NALVNPQELV LLRGIVKFET PNPYINKFAG KVEVTVSEGC GMEVMPLSVK NVLLRGCNLR
NTDWVFGLVL NTGPDTKIMQ SASAAPSKWS DVMLSMNKMI AILCLGLFVA CAVAATCYVT
WQYDIVRNTW YIKLSDDVRA QPRWESFIQM MFYYFLLLYQ VIPISLYVSM TSVKFLQAKF
MVWDLEMYHA ETDTPAIVRT MALNEELGQI SYVFSDKTGT LTCNIMEFRK CSINGISYGS
GMTEIGRAAL VRANKPIPPE PKMDAGMKKM QYVNFVDPSF FKAMNGGTGA AQRDNIHQFF
EHLAVCHTVI PEKLETGEVR LSASSPDEQA LVAGASFVGF NFVNRGVGKA TIEIFGERQV
FDILDVLEFN STRKRMSVVV RRPNGELYLY SKGADMMIYQ RLKDDPAMDQ LKKVTRDHME
KYADDGLRTL ALAVKKLDEK WFQKWKIKFD EAQGNVAELD RRKDGKPNAI DSLMEEIEEN
LELIGATAIE DKLQDGVPKC LAHLTAAGIK VWMLTGDKEE TAINIAYACS LLDNSIQQVI
VNCTTCPNEE AIIARLNAAG REYREKTKAD SKLEISLIID GEALEWALSP RTAPHLLEFT
KLCRAVICNR VSPAQKAEMV RLVRDNIPVA RTLAIGDGAN DVAMIQAAHV GVGISGQEGM
QAVNSSDYAI AQFRFLERLL LVHGRWNYIR ISKLVLYMFY KNITLVLAQY WYGYLSGASG
SKMYWELGVQ VYNVAFTGIP IIMVGVMDKD LPARFSIEYP DLYRKGPERY YFNMYTFLRW
VGAAVFESLV IFVVMSYGFN ASESAPGSES RVEYGMVAFS MTVLIVNIKI WLISDTWTFL
SLICWSLSVL SWFGFAAMGT EVTFFSRFKV AYDEFGSFAP TAWSWGYVLV VLMGCVIALG
RHFTYNQYQR AFYPELNQVL QESVEKRKRR LTINHIEEQT LSMSLDDVHA TAFMSDFRGT
DLTVKSYRTN SGGVNMHDAI AEDEIYESSG GGVPSLAMSD NVSLTADSFS ASVYSSSVSS
EVGSGWDRIP TKLFKSNASR RNTGYAFSCD EETTLAESYI ASNSLPRSDA VPAALRNSIS
RHMS
//
